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Published online
doi:10.1083/jcb.200807023
The Journal of Cell Biology, Vol. 183, No. 7, 1287-1298
The Rockefeller University Press, 0021-9525 $30.00
© Lewkowicz et al.
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Article

The microtubule-binding protein CLIP-170 coordinates mDia1 and actin reorganization during CR3-mediated phagocytosis



Elodie Lewkowicz1,2, Floriane Herit1,2, Christophe Le Clainche3, Pierre Bourdoncle1,2, Franck Perez4,5, and Florence Niedergang1,2

1 Institut Cochin, Université Paris Descartes, Centre National de la Recherche Scientifique, Unité Mixte de Recherche 8104, 75014 Paris, France
2 Institut national de la santé et de la recherche médicale, Unité 567, 75014 Paris, France
3 Centre National de la Recherche Scientifique, Unité Propre de Recherche 3082, 91190 Gif-sur-Yvette, France
4 Institut Curie, Centre de Recherche, 75248 Paris, France
5 Centre National de la Recherche Scientifique, Unité Mixte de Recherche 144, 75248 Paris, France

Correspondence to Florence Niedergang: florence.niedergang{at}inserm.fr

Microtubule dynamics are modulated by regulatory proteins that bind to their plus ends (+TIPs [plus end tracking proteins]), such as cytoplasmic linker protein 170 (CLIP-170) or end-binding protein 1 (EB1). We investigated the role of +TIPs during phagocytosis in macrophages. Using RNA interference and dominant-negative approaches, we show that CLIP-170 is specifically required for efficient phagocytosis triggered by {alpha}Mβ2 integrin/complement receptor activation. This property is not observed for EB1 and EB3. Accordingly, whereas CLIP-170 is dynamically enriched at the site of phagocytosis, EB1 is not. Furthermore, we observe that CLIP-170 controls the recruitment of the formin mDia1, an actin-nucleating protein, at the onset of phagocytosis and thereby controls actin polymerization events that are essential for phagocytosis. CLIP-170 directly interacts with the formin homology 2 domain of mDia1. The interaction between CLIP-170 and mDia1 is negatively regulated during {alpha}Mβ2-mediated phagocytosis. Our results unravel a new microtubule/actin cooperation that involves CLIP-170 and mDia1 and that functions downstream of {alpha}Mβ2 integrins.

Abbreviations used in this paper: CLIP, cytoplasmic linker protein; CR3, complement receptor 3; DAD, diaphanous autoregulatory domain; EB, end-binding protein; FcR, Fc receptor; FH2, formin homology 2; shRNA, small hairpin RNA; SRBC, sheep red blood cell.

© 2008 Lewkowicz et al. This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.jcb.org/misc/terms.shtml). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 3.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/3.0/).


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